L. Mcneil et al., IDENTIFICATION, CHARACTERIZATION, AND DEVELOPMENTAL REGULATION OF A RECEPTOR GUANYLYL CYCLASE EXPRESSED DURING EARLY STAGES OF DROSOPHILA DEVELOPMENT, The Journal of biological chemistry, 270(13), 1995, pp. 7189-7196
Membrane forms of guanylyl cyclase are single-transmembrane proteins t
hat are activated by the binding of specific peptide ligands to their
extracellular domains. In this report, we describe the identification
and characterization of a Drosophila cDNA clone encoding a protein, Dr
GC-1, with high sequence identity to members of this family of recepto
r proteins, The protein contains a single, hydrophobic domain predicte
d to represent a transmembrane segment separating an extracellular dom
ain with significant sequence identity (30%) to sea urchin egg peptide
receptors from intracellular domains containing a protein kinase-like
domain followed by a region with high sequence identity (65%) to cycl
ase catalytic domains found in receptor guanylyl cyclases from both ve
rtebrates and invertebrates. In contrast to other members of this fami
ly, DrGC-1 is predicted to contain a carboxyl-terminal extension of 43
0 residues that has no homology to any described protein. Northern ana
lysis indicates that DrGC-1 transcripts are present at variable levels
in all stages of development. In situ hybridization demonstrates that
high levels of uniformly distributed transcript are present in 0-2-h
embryos. Later in embryogenesis (14-18 h), elevated levels of hybridiz
ation appear to be preferentially associated with muscle fibers.